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Blanke, Kristina
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Novick, Rachel
 Rachel Novick - Email
PhD Candidate - Started in 2004
Native of Massachusetts
Lab of Adnan Elfarra, PhD
President of METC Student Liaison Committee (2007-08)
Undergraduate Work
Washington University in St. Louis (1998-2002)
B.A. Biology
B.A. Environmental Science
Research (updated 03/2009)
Flavin-containing monooxygenases (FMOs) are a family of microsomal proteins that catalyze the oxidation of many pharmaceutical drugs, pesticides, and endogenous compounds. Generally, FMO oxidation aids in excretion and detoxification; however, some substrates may be bioactivated to more reactive metabolites. In humans, five expressed FMO isoforms (FMO 1-5) and six non-expressed pseudogenes (FMO6P-11P) have been detected. Each FMO isoform exhibits distinct substrate specificity and sex-, tissue-, age-, and species-dependent expression patterns.
My research project is to investigate the physical, immunological, and enzymatic properties of different FMO isoforms to elucidate their role in oxidative metabolism.
Renal FMO3 was purified via affinity columns based on the elution of L-methionine S-oxidase activity. The resulting protein was subjected to trypsin digestion and MALDI-TOF mass spectral analysis, 34% of the sequence of rat FMO3 was detected. The apparent Km and Vmax values for rat kidney FMO3 were determined with methionine, seleno-L-methionine, S-allyl-L-cysteine, and methimazole. The stereoselectivity of the reactions with methionine and S-allyl-cysteine were examined. We are also characterizing FMO4 to elucidate its role in oxidative metabolism.
We examined the regional distribution of FMO isoforms 1, 3, and 4 in rat liver and kidney using immunohistochemistry. Rabbit polyclonal antibodies to rat FMO1 and FMO4 were developed using antipeptide technology. Specificities of the antibodies were verified using western blotting, immunoprecipitation, and IHC. This data provided a compelling visual demonstration of the isoform-specific localization patterns of FMO1, 3 and 4 in the rat liver and kidney . The FMO4 antibody reacted with mouse and human tissues providing the first evidence for expression of FMO4 at the protein level in mouse and human liver and kidney microsomes.
 Funding & Awards
National Research Service Award Predoctoral Traineeship (NIEHS Training Grant T32, Feb 2005-2008)
Vilas Travel Fellowship - March 2008 & March 2009
Society of Toxicology Travel Award - March 2008
Memberships
Society of Toxicology (2008)
Hobbies/Interests
Running, hiking, tennis, and reading
Posters
- Novick RM, Mitzey AM, Brownfield MS, Elfarra AA. Differential Localization of Flavin-Containing Monooxygenase Isoforms 1, 3, and 4 in Rat Liver and Kidney. Poster presentation at the Society of Toxicology Meeting in Baltimore, MD 2009.
- Novick RM, Elfarra AA. Purification and characterization of flavin-containing monooxygenase isoform 3 from rat kidney microsomes. Poster presentation at the Society of Toxicology meeting in Seattle, WA 2008.
Publications- Novick RM, Mitzey AM, Brownfield MS, Elfarra AA. Differential Localization of Flavin-Containing Monooxygenase Isoforms 1, 3, and 4 in Rat Liver and Kidney and
Evidence for Expression of FMO4 in Mouse, Rat, and Human Liver and Kidney Microsomes. J Pharmacol Exp Ther. 2009 Mar 23. 1148-1155 - Novick RM, Elfarra AA. Purification and characterization of flavin-containing monooxygenase isoform 3 from rat kidney microsomes. Drug Metab Dispos. 2008 Dec;36(12):2468-74.
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